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3eqn
From Proteopedia
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| - | [[Image:3eqn.png|left|200px]] | ||
| - | < | + | ==Crystal structure of beta-1,3-glucanase from Phanerochaete chrysosporium (Lam55A)== |
| - | + | <StructureSection load='3eqn' size='340' side='right'caption='[[3eqn]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3eqn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EQN FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eqn OCA], [https://pdbe.org/3eqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eqn RCSB], [https://www.ebi.ac.uk/pdbsum/3eqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eqn ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q2Z1W1_PHACH Q2Z1W1_PHACH] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eq/3eqn_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3eqn ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycoside hydrolase family 55 consists of beta-1,3-glucanases mainly from filamentous fungi. A beta-1,3-glucanase (Lam55A) from the Basidiomycete Phanerochaete chrysosporium hydrolyzes beta-1,3-glucans in the exo-mode with inversion of anomeric configuration and produces gentiobiose in addition to glucose from beta-1,3/1,6-glucans. Here we report the crystal structure of Lam55A, establishing the three-dimensional structure of a member of glycoside hydrolase 55 for the first time. Lam55A has two beta-helical domains in a single polypeptide chain. These two domains are separated by a long linker region but are positioned side by side, and the overall structure resembles a rib cage. In the complex, a gluconolactone molecule is bound at the bottom of a pocket between the two beta-helical domains. Based on the position of the gluconolactone molecule, Glu-633 appears to be the catalytic acid, whereas the catalytic base residue could not be identified. The substrate binding pocket appears to be able to accept a gentiobiose unit near the cleavage site, and a long cleft runs from the pocket, in accordance with the activity of this enzyme toward various beta-1,3-glucan oligosaccharides. In conclusion, we provide important features of the substrate-binding site at the interface of the two beta-helical domains, demonstrating an unexpected variety of carbohydrate binding modes. | ||
| - | + | Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.,Ishida T, Fushinobu S, Kawai R, Kitaoka M, Igarashi K, Samejima M J Biol Chem. 2009 Apr 10;284(15):10100-9. Epub 2009 Feb 4. PMID:19193645<ref>PMID:19193645</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3eqn" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |
| - | + | *[[Glucanase 3D structures|Glucanase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | [[ | + | [[Category: Large Structures]] |
| - | + | [[Category: Phanerodontia chrysosporium]] | |
| - | == | + | [[Category: Fushinobu S]] |
| - | < | + | [[Category: Igarashi K]] |
| - | [[Category: | + | [[Category: Ishida T]] |
| - | [[Category: | + | [[Category: Kawai R]] |
| - | [[Category: Fushinobu | + | [[Category: Kitaoka M]] |
| - | [[Category: Igarashi | + | [[Category: Samejima M]] |
| - | [[Category: Ishida | + | |
| - | [[Category: Kawai | + | |
| - | [[Category: Kitaoka | + | |
| - | [[Category: Samejima | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of beta-1,3-glucanase from Phanerochaete chrysosporium (Lam55A)
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